ID SSB_MYCTU Reviewed; 164 AA. AC P9WGD5; L0T5J5; P0A610; P71711; DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot. DT 16-APR-2014, sequence version 1. DT 02-OCT-2024, entry version 52. DE RecName: Full=Single-stranded DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_00984}; DE Short=SSB {ECO:0000255|HAMAP-Rule:MF_00984}; GN Name=ssb {ECO:0000303|PubMed:10491108}; OrderedLocusNames=Rv0054; GN ORFNames=MTCY21D4.17; OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium tuberculosis complex. OX NCBI_TaxID=83332; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25618 / H37Rv; RX PubMed=9634230; DOI=10.1038/31159; RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K., RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., RA Barrell B.G.; RT "Deciphering the biology of Mycobacterium tuberculosis from the complete RT genome sequence."; RL Nature 393:537-544(1998). RN [2] RP SSDNA-BINDING, AND SUBUNIT. RX PubMed=10491108; DOI=10.1046/j.1432-1327.1999.00684.x; RA Purnapatre K., Varshney U.; RT "Cloning, over-expression and biochemical characterization of the single- RT stranded DNA binding protein from Mycobacterium tuberculosis."; RL Eur. J. Biochem. 264:591-598(1999). RN [3] RP SSDNA-BINDING. RC STRAIN=ATCC 25618 / H37Rv; RX PubMed=20724443; DOI=10.1093/nar/gkq737; RA Huang F., He Z.G.; RT "Characterization of an interplay between a Mycobacterium tuberculosis MazF RT homolog, Rv1495 and its sole DNA topoisomerase I."; RL Nucleic Acids Res. 38:8219-8230(2010). RN [4] RP CRYSTALLIZATION, AND SUBUNIT. RX PubMed=12888346; DOI=10.1016/s0022-2836(03)00729-0; RA Saikrishnan K., Jeyakanthan J., Venkatesh J., Acharya N., Sekar K., RA Varshney U., Vijayan M.; RT "Structure of Mycobacterium tuberculosis single-stranded DNA-binding RT protein. Variability in quaternary structure and its implications."; RL J. Mol. Biol. 331:385-393(2003). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=ATCC 25618 / H37Rv; RX PubMed=21969609; DOI=10.1074/mcp.m111.011445; RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K., RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R., RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M., RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.; RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution RT mass spectrometry."; RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011). RN [6] RP INTERACTION WITH DNAB, SSDNA-BINDING, AND MUTAGENESIS OF ASN-12; PHE-21; RP PRO-132; 145-PRO--PHE-164 AND 155-PHE--PHE-165. RX PubMed=24387047; DOI=10.1111/febs.12703; RA Zhang H., Zhang Z., Yang J., He Z.G.; RT "Functional characterization of DnaB helicase and its modulation by single- RT stranded DNA binding protein in Mycobacterium tuberculosis."; RL FEBS J. 281:1256-1266(2014). CC -!- FUNCTION: Binds single-stranded (ss)DNA (PubMed:10491108, CC PubMed:20724443, PubMed:24387047). At low concentrations (0.02 to 0.16 CC uM), stimulates the 5'-3' helicase activity of DnaB (PubMed:24387047). CC At higher concentrtions eventually totally inhibits DnaB helicase CC (PubMed:24387047). {ECO:0000269|PubMed:10491108, CC ECO:0000269|PubMed:20724443, ECO:0000269|PubMed:24387047}. CC -!- SUBUNIT: Homotetramer (PubMed:10491108, PubMed:12888346). Interacts CC with DnaB (PubMed:24387047). {ECO:0000255|HAMAP-Rule:MF_00984, CC ECO:0000269|PubMed:10491108, ECO:0000269|PubMed:12888346, CC ECO:0000269|PubMed:24387047}. CC -!- INTERACTION: CC P9WGD5; P9WMR3: dnaB; NbExp=3; IntAct=EBI-9081374, EBI-9081402; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL123456; CCP42776.1; -; Genomic_DNA. DR PIR; F70913; F70913. DR RefSeq; NP_214568.1; NC_000962.3. DR RefSeq; WP_003400534.1; NZ_NVQJ01000005.1. DR PDB; 1UE1; X-ray; 2.50 A; A/B=1-164. DR PDB; 1UE5; X-ray; 2.60 A; A/B=1-164. DR PDB; 1UE6; X-ray; 2.70 A; A/B/C/D=1-164. DR PDB; 1UE7; X-ray; 3.20 A; A/B/C/D=1-164. DR PDB; 7F5Y; X-ray; 1.92 A; A/B=1-164. DR PDB; 7F5Z; X-ray; 3.00 A; A/B=1-164. DR PDBsum; 1UE1; -. DR PDBsum; 1UE5; -. DR PDBsum; 1UE6; -. DR PDBsum; 1UE7; -. DR PDBsum; 7F5Y; -. DR PDBsum; 7F5Z; -. DR AlphaFoldDB; P9WGD5; -. DR SASBDB; P9WGD5; -. DR SMR; P9WGD5; -. DR IntAct; P9WGD5; 1. DR MINT; P9WGD5; -. DR STRING; 83332.Rv0054; -. DR PaxDb; 83332-Rv0054; -. DR DNASU; 887013; -. DR GeneID; 887013; -. DR KEGG; mtu:Rv0054; -. DR TubercuList; Rv0054; -. DR eggNOG; COG0629; Bacteria. DR InParanoid; P9WGD5; -. DR OrthoDB; 9809878at2; -. DR PhylomeDB; P9WGD5; -. DR EvolutionaryTrace; P9WGD5; -. DR Proteomes; UP000001584; Chromosome. DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE. DR GO; GO:0009295; C:nucleoid; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE. DR GO; GO:0003697; F:single-stranded DNA binding; IDA:MTBBASE. DR GO; GO:0006974; P:DNA damage response; IEP:MTBBASE. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR GO; GO:0046677; P:response to antibiotic; IEP:MTBBASE. DR CDD; cd04496; SSB_OBF; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1. DR HAMAP; MF_00984; SSB; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR000424; Primosome_PriB/ssb. DR InterPro; IPR011344; ssDNA-bd. DR NCBIfam; TIGR00621; ssb; 1. DR PANTHER; PTHR10302; SINGLE-STRANDED DNA-BINDING PROTEIN; 1. DR PANTHER; PTHR10302:SF27; SINGLE-STRANDED DNA-BINDING PROTEIN; 1. DR Pfam; PF00436; SSB; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1. DR PROSITE; PS50935; SSB; 1. PE 1: Evidence at protein level; KW 3D-structure; DNA-binding; Reference proteome. FT CHAIN 1..164 FT /note="Single-stranded DNA-binding protein" FT /id="PRO_0000096069" FT DOMAIN 1..110 FT /note="SSB" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00984" FT REGION 120..164 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 121..145 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MUTAGEN 12 FT /note="N->S: 2-fold increase of stimulation of DnaB FT helicase activity; when associated with L-132." FT /evidence="ECO:0000269|PubMed:24387047" FT MUTAGEN 21 FT /note="F->L: No longer stimulates DnaB helicase activity." FT /evidence="ECO:0000269|PubMed:24387047" FT MUTAGEN 132 FT /note="P->L: 2-fold increase of stimulation of DnaB FT helicase activity; when associated with S-12." FT /evidence="ECO:0000269|PubMed:24387047" FT MUTAGEN 145..164 FT /note="Missing: Loss of interaction with DnaB, weakly FT stimulates helicase activity of DnaB." FT /evidence="ECO:0000269|PubMed:24387047" FT MUTAGEN 155..164 FT /note="Missing: Still interacts with DnaB." FT /evidence="ECO:0000269|PubMed:24387047" FT STRAND 6..15 FT /evidence="ECO:0007829|PDB:7F5Y" FT STRAND 18..21 FT /evidence="ECO:0007829|PDB:7F5Y" FT TURN 23..25 FT /evidence="ECO:0007829|PDB:1UE7" FT STRAND 27..35 FT /evidence="ECO:0007829|PDB:7F5Y" FT STRAND 39..41 FT /evidence="ECO:0007829|PDB:7F5Y" FT TURN 42..45 FT /evidence="ECO:0007829|PDB:7F5Y" FT STRAND 53..60 FT /evidence="ECO:0007829|PDB:7F5Y" FT HELIX 61..70 FT /evidence="ECO:0007829|PDB:7F5Y" FT STRAND 76..88 FT /evidence="ECO:0007829|PDB:7F5Y" FT STRAND 91..93 FT /evidence="ECO:0007829|PDB:1UE5" FT STRAND 94..108 FT /evidence="ECO:0007829|PDB:7F5Y" FT STRAND 110..118 FT /evidence="ECO:0007829|PDB:7F5Y" SQ SEQUENCE 164 AA; 17353 MW; 14797F8379FC2036 CRC64; MAGDTTITIV GNLTADPELR FTPSGAAVAN FTVASTPRIY DRQTGEWKDG EALFLRCNIW REAAENVAES LTRGARVIVS GRLKQRSFET REGEKRTVIE VEVDEIGPSL RYATAKVNKA SRSGGFGSGS RPAPAQTSSA SGDDPWGSAP ASGSFGGGDD EPPF //